Collagenolytic serine protease PC and trypsin PC from king crab Paralithodes camtschaticus: cDNA cloning and primary structure of the enzymes.

ABSTRACT:

Background

In this paper, we describe cDNA cloning of a new anionic trypsin and a collagenolytic serine protease from king crab Paralithodes camtschaticus and the elucidation of their primary structures. Constructing the phylogenetic tree of these enzymes was undertaken in order to prove the evolutionary relationship between them.

Results

The mature trypsin PC and collagenolytic protease PC contain 237 (Mcalc 24.8 kDa) and 226 amino acid residues (Mcalc 23.5 kDa), respectively. Alignments of their amino acid sequences revealed a high degree of the trypsin PC identity to the trypsin from Penaeus vannamei (approximately 70%) and of the collagenolytic protease PC identity to the collagenase from fiddler crab Uca pugilator (76%). The phylogenetic tree of these enzymes was constr

SUBMITTER: Rudenskaya GN 

PROVIDER: S-EPMC343286 | biostudies-literature | 2004 Jan

REPOSITORIES: biostudies-literature